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3CMQ

Crystal structure of human mitochondrial phenylalanine tRNA synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004826molecular_functionphenylalanine-tRNA ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006432biological_processphenylalanyl-tRNA aminoacylation
A0008033biological_processtRNA processing
A0043039biological_processtRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 416
ChainResidue
AGLY254

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FA5 A 999
ChainResidue
AGLN157
AGLU159
APHE234
AGLU251
AGLY277
AARG282
AILE293
AHOH1008
AHOH1025
AHOH1051
AHIS119
AHOH1116
ASER121
AGLN124
AARG143
AGLN150
AHIS151
ATYR152
APHE155

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues13
DetailsLIPOCALIN Lipocalin signature. EMEi.NFHGEWLEV
ChainResidueDetails
AGLU240-VAL252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ASER121
AGLN150
AGLN157

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18611382, ECO:0000269|PubMed:19549855
ChainResidueDetails
AARG143
AGLU251
APHE276

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS166

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b7y
ChainResidueDetails
AARG143
AALA275

219140

PDB entries from 2024-05-01

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